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Mouse Anti-FUT3 Recombinant Antibody (CBXS-0022) (CBMAB-S3027-CQ)

This product is a mouse antibody that recognizes FUT3. The antibody CBXS-0022 can be used for immunoassay techniques such as: WB, ICC, IHC-P, IHC-Fr, ELISA.
See all FUT3 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBXS-0022
Application
WB, ICC, IHC-P, IHC-Fr, ELISA

Basic Information

Immunogen
Carbohydrate Antigen 19-9
Specificity
Human
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4, 50% glycerol
Preservative
0.02% sodium azide
Concentration
0.5 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Fucosyltransferase 3 (Lewis Blood Group)
Introduction
The Lewis histo-blood group system comprises a set of fucosylated glycosphingolipids that are synthesized by exocrine epithelial cells and circulate in body fluids. The glycosphingolipids function in embryogenesis, tissue differentiation, tumor metastasis, inflammation, and bacterial adhesion. They are secondarily absorbed to red blood cells giving rise to their Lewis phenotype. This gene is a member of the fucosyltransferase family, which catalyzes the addition of fucose to precursor polysaccharides in the last step of Lewis antigen biosynthesis. It encodes an enzyme with alpha(1,3)-fucosyltransferase and alpha(1,4)-fucosyltransferase activities. Mutations in this gene are responsible for the majority of Lewis antigen-negative phenotypes. Multiple alternatively spliced variants, encoding the same protein, have been found for this gene.
Entrez Gene ID
2525
UniProt ID
P21217
Alternative Names
Fucosyltransferase 3 (Lewis Blood Group); Blood Group Lewis Alpha-4-Fucosyltransferase; Galactoside 3(4)-L-Fucosyltransferase; Fucosyltransferase III; EC 2.4.1.65; Lewis FT; FucT-III; FT3B; LE;
Function
Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors and participates in the blood groups Lewis determination and expression of Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens (PubMed:12668675, PubMed:1977660, PubMed:11058871).

Also catalyzes the transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sialyl Lewis a expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration (PubMed:12668675, PubMed:11058871, PubMed:27453266).

Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin (PubMed:11058871).

Prefers type 1 chain over type 2 acceptors (PubMed:7721776).

Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred (PubMed:7721776).

Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme (PubMed:1977660).
Biological Process
Cell-cell recognition Source: BHF-UCL
Ceramide metabolic process Source: BHF-UCL
Fucosylation Source: UniProtKB
Macromolecule glycosylation Source: BHF-UCL
Oligosaccharide biosynthetic process Source: BHF-UCL
Oligosaccharide metabolic process Source: UniProtKB
Positive regulation of cell-cell adhesion Source: UniProtKB
Protein glycosylation Source: UniProtKB-UniPathway
Regulation of cell migration Source: UniProtKB
Regulation of cell population proliferation Source: UniProtKB
Cellular Location
Golgi stack membrane. Membrane-bound form in trans cisternae of Golgi.
Topology
Cytoplasmic: 1-15
Helical: 16-34
Lumenal: 35-361
PTM
Glycosylated.

Kløve‐Mogensen, K., Steffensen, R., Masmas, T. N., Glenthøj, A., Haunstrup, T. M., Ratcliffe, P., ... & Nielsen, K. R. (2022). ABO, secretor, and Lewis carbohydrate histo‐blood groups are associated with autoimmune neutropenia of early childhood in Danish patients. Transfusion, 62(8), 1636-1642.

Matzhold, E. M., Berghold, A., Bemelmans, M. K. B., Banfi, C., Stelzl, E., Kessler, H. H., ... & Wagner, T. (2021). Lewis and ABO histo‐blood types and the secretor status of patients hospitalized with COVID‐19 implicate a role for ABO antibodies in susceptibility to infection with SARS‐CoV‐2. Transfusion, 61(9), 2736-2745.

Boniface, K., Byars, S. G., Cowley, D., Kirkwood, C. D., & Bines, J. E. (2020). Human neonatal rotavirus vaccine (RV3-BB) produces vaccine take irrespective of histo-blood group antigen status. The Journal of Infectious Diseases, 221(7), 1070-1078.

Ramani, S., & Giri, S. (2019). Influence of histo blood group antigen expression on susceptibility to enteric viruses and vaccines. Current Opinion in Infectious Diseases, 32(5), 445-452.

Colston, J. M., Francois, R., Pisanic, N., Peñataro Yori, P., McCormick, B. J., Olortegui, M. P., ... & Kosek, M. N. (2019). Effects of child and maternal histo-blood group antigen status on symptomatic and asymptomatic enteric infections in early childhood. The Journal of infectious diseases, 220(1), 151-162.

King, J. R., Varadé, J., & Hammarström, L. (2019). Fucosyltransferase gene polymorphisms and Lewisb-negative status are frequent in Swedish newborns, with implications for infectious disease susceptibility and personalized medicine. Journal of the Pediatric Infectious Diseases Society, 8(6), 507-518.

Barbé, L., Le Moullac-Vaidye, B., Echasserieau, K., Bernardeau, K., Carton, T., Bovin, N., ... & Le Pendu, J. (2018). Histo-blood group antigen-binding specificities of human rotaviruses are associated with gastroenteritis but not with in vitro infection. Scientific reports, 8(1), 12961.

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For research use only. Not intended for any clinical use.

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